ID   PYRB1_PEA               Reviewed;         386 AA.
AC   Q43086;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Aspartate carbamoyltransferase 1, chloroplastic;
DE            EC=2.1.3.2;
DE   AltName: Full=Aspartate transcarbamylase 1;
DE            Short=ATCase 1;
DE   Flags: Precursor;
GN   Name=PYRB1;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Wando; TISSUE=Leaf;
RX   PubMed=8029359; DOI=10.1104/pp.105.1.377;
RA   Williamson C.L., Slocum R.D.;
RT   "Molecular cloning and characterization of the pyrB1 and pyrB2 genes
RT   encoding aspartate transcarbamoylase in pea (Pisum sativum L.).";
RL   Plant Physiol. 105:377-384(1994).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC         aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58228; EC=2.1.3.2;
CC   -!- ACTIVITY REGULATION: Allosterically regulated by UMP.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 2/3.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. ATCase family. {ECO:0000305}.
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DR   EMBL; M96981; AAA62443.1; -; mRNA.
DR   PIR; T06484; T06484.
DR   AlphaFoldDB; Q43086; -.
DR   SMR; Q43086; -.
DR   EnsemblPlants; Psat2g012520.1; Psat2g012520.1.cds; Psat2g012520.
DR   EnsemblPlants; Psat2g012520.2; Psat2g012520.2.cds; Psat2g012520.
DR   Gramene; Psat2g012520.1; Psat2g012520.1.cds; Psat2g012520.
DR   Gramene; Psat2g012520.2; Psat2g012520.2.cds; Psat2g012520.
DR   UniPathway; UPA00070; UER00116.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1370; -; 2.
DR   HAMAP; MF_00001; Asp_carb_tr; 1.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR   InterPro; IPR002082; Asp_carbamoyltransf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   SUPFAM; SSF53671; SSF53671; 1.
DR   TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE   2: Evidence at transcript level;
KW   Allosteric enzyme; Chloroplast; Plastid; Pyrimidine biosynthesis;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..386
FT                   /note="Aspartate carbamoyltransferase 1, chloroplastic"
FT                   /id="PRO_0000020349"
SQ   SEQUENCE   386 AA;  42618 MW;  A9440F45474E29F4 CRC64;
     MTVASMLSSN SMNVGVSNPK MSSKTSACCL LNRPWPSSCS MSISSCGQFG VSEKSKLLCG
     AGALQVESAP LFSVGQKFQL DDVIEAQQFD RETLSAIFEV ARSMENIRGN SSGSQMLKGY
     LMATLFYEPS TRTRLSFESA MKRLGGDVLT TENAREFSSA AKGETLEDTI RTVEGYSDII
     VLRHFESGAA RRAAATANIP VINAGDGPGQ HPSQALLDVY TIEREIGKLD GIKVGLVGDL
     ANGRTVRSLA YLLAKYRDVK LYFVSPNVVK MKDDIKEYLT SKGVEWEESS DLMEVASKCD
     VVYQTRIQKE RFGEKLNLYE EARGKYIVNQ DVLKVMQNHA VVMHPLPKLD EIEADVDNDP
     RAAYFRQAKN GLYIRMALLK VLLLGW